Abstract
GMP-140 is an integral membrane glycoprotein found in secretory granules of platelets and endothelial cells. After cellular activation, it is rapidly redistributed to the plasma membrane. The cDNA-derived primary structure of GMP-140 predicts a cysteine-rich protein with multiple domains, including a "lectin" region, an "EGF" domain, nine tandem consensus repeats related to those in complement-binding proteins, a transmembrane domain, and a short cytoplasmic tail. Some cDNAs also predict a soluble protein with a deleted transmembrane segment. The domain organization of GMP-140 is similar to that of ELAM-1, a cytokine-inducible endothelial cell receptor that binds neutrophils. This similarity suggests that GMP-140 belongs to a new family of inducible receptors with related structure and function on vascular cells.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Blotting, Northern
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Blotting, Southern
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Cell Adhesion*
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Cloning, Molecular*
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Cytoplasmic Granules / analysis*
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Cytoplasmic Granules / ultrastructure
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DNA / analysis
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DNA / isolation & purification
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Endothelium, Vascular / analysis*
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Endothelium, Vascular / cytology
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Endothelium, Vascular / ultrastructure
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Homeostasis
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Humans
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Inflammation / metabolism
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Inflammation / physiopathology*
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Intracellular Membranes / analysis
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Megakaryocytes / analysis*
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Megakaryocytes / cytology
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Megakaryocytes / ultrastructure
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Membrane Proteins / analysis*
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Membrane Proteins / genetics
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Membrane Proteins / physiology
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Molecular Sequence Data
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P-Selectin
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Platelet Membrane Glycoproteins / analysis
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Platelet Membrane Glycoproteins / genetics*
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Platelet Membrane Glycoproteins / physiology
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Protein Biosynthesis
Substances
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Membrane Proteins
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P-Selectin
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Platelet Membrane Glycoproteins
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DNA